Type

Journal Article

Authors

Maria Hayes
Pádraigín Harnedy
Anne Maria Mullen
Eileen O'Neill
Joseph Kerry
Declan Bolton
Dilip K Rai
Roberta Di Bernardini

Subjects

Chemistry

Topics
peptides ferrous compounds protein hydrolysates water thermolysin free radical scavengers beta globins pulmonary surfactant associated protein a proteins filtration alpha globins biphenyl compounds fatty acid binding proteins cattle chemistry nitrogen amino acid sequence iron chelating agents metabolism ferric chloride chlorides spectrometry mass electrospray ionization liver extracts ferrous chloride ferric compounds snrnp core proteins catalase cytoplasm antioxidants large conductance calcium activated potassium channel alpha subunits picrates chromatography high pressure liquid animals 2 2 diphenyl 1 picrylhydrazyl

Isolation, purification and characterization of antioxidant peptidic fractions from a bovine liver sarcoplasmic protein thermolysin hydrolyzate. (2010)

Abstract Sarcoplasmic proteins isolated from bovine livers were hydrolyzed using the enzyme thermolysin at 37°C for 2h. The hydrolyzates were filtered through molecular weight cut off membranes (MWCO) and filtrates were obtained. The water activity (a(w)) of unhydrolysed sarcoplasmic protein, full hydrolyzates, 10-kDa and 3-kDa filtrates were below the limit necessary for microbial growth. The antioxidant activities of both filtrates and fractions were assessed using the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity assay, the ferric ion reducing antioxidant power (FRAP) assay and the Fe(2+) chelating ability assay. RP-HPLC was used for purification of the full hydrolyzates, the 10-kDa and the 3-kDa filtrates. The peptidic content of the full hydrolyzates, the 10-kDa and the 3-kDa filtrates were assessed using the Dumas method and peptide contents of each fraction were characterized using electrospray quadrupole time-of-flight (ESI-Q-TOF) mass spectrometry with the resultant spectrum analysed using the software programmes Protein Lynx Global Server 2.4. and TurboSEQUEST. Similarities between the amino acid composition of characterized peptides from each fraction and previously reported antioxidant peptides were found. This study demonstrates that meat by-product such as liver can be utilised as raw material for the generation of bioactive peptides with demonstrated antioxidant activities in vitro using the enzyme thermolysin. It is significant as it presents a potential opportunity for meat processors to use their waste streams for the generation of bioactive peptides for potential functional food use.
Collections Ireland -> Teagasc -> PubMed

Full list of authors on original publication

Maria Hayes, Pádraigín Harnedy, Anne Maria Mullen, Eileen O'Neill, Joseph Kerry, Declan Bolton, Dilip K Rai, Roberta Di Bernardini

Experts in our system

1
Maria Hayes
Teagasc
Total Publications: 34
 
2
Anne Maria Mullen
Teagasc
Total Publications: 50
 
4
J P Kerry
University College Cork
Total Publications: 130
 
5
D J Bolton
Teagasc
Total Publications: 96
 
6
Dilip K. Rai
Teagasc
Total Publications: 53